PKN1_MOUSE - dbPTM
PKN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKN1_MOUSE
UniProt AC P70268
Protein Name Serine/threonine-protein kinase N1
Gene Name Pkn1
Organism Mus musculus (Mouse).
Sequence Length 946
Subcellular Localization Cytoplasm . Nucleus . Endosome . Cell membrane
Peripheral membrane protein. Cleavage furrow . Midbody . Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the
Protein Description PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro..
Protein Sequence MAGDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLKREIRKELKLKEGAENLRRATTDLGRSLAPVELLLRGSARRLDLLHQQLQELHAHVVLPDPAAGSDATQSLAEGSPICSSTNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSSKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQALQAGELESQAAPDEAQGDPELGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSGAKAPDRKAVSEAQEKLTESNQKLGLLRESLERRLGELPADHPKGRLLREELTAASSSAFSAILPGPFPATHYSTLSKPAPLTGTLEVRVVGCKNLPETIPWSPPPSVGASGTPESRTPFLSRPARGLYSRSGSLSGRSSLRGEAENATEVSTVLKLDNTVVGQTAWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPIIERIPRLQRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPSAVATGTFSPNASPGAEIRHTGDISMEKLNLGADSDSSSQKSPPGLPSTSCSLSSPTHESTTSPELPSETQETPGPGLCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRSSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTRAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSTERDAEDVKKQPFFRSLGWDVLLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFRDFDFVAGGY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAGDAVQSE
------CCCHHHCCC		25.27-
8PhosphorylationMAGDAVQSEPRSWSL
CCCHHHCCCCCHHHH		42.8620139300
63PhosphorylationAENLRRATTDLGRSL
HHHHHHHHHHHCCCC		21.02-
64PhosphorylationENLRRATTDLGRSLA
HHHHHHHHHHCCCCH		28.3922322096
69PhosphorylationATTDLGRSLAPVELL
HHHHHCCCCHHHHHH		27.38-
243PhosphorylationKNVLRLLSGAKAPDR
HHHHHHHHCCCCCCH		41.1026643407
273PhosphorylationKLGLLRESLERRLGE
HHHHHHHHHHHHHCC		29.1519854140
342PhosphorylationGCKNLPETIPWSPPP
EECCCCCCCCCCCCC		30.3330372032
346PhosphorylationLPETIPWSPPPSVGA
CCCCCCCCCCCCCCC		23.3627180971
350PhosphorylationIPWSPPPSVGASGTP
CCCCCCCCCCCCCCC		38.6726745281
354PhosphorylationPPPSVGASGTPESRT
CCCCCCCCCCCCCCC		36.9526745281
356PhosphorylationPSVGASGTPESRTPF
CCCCCCCCCCCCCCC		22.7626643407
359PhosphorylationGASGTPESRTPFLSR
CCCCCCCCCCCCCCC		42.5326643407
369MethylationPFLSRPARGLYSRSG
CCCCCCCCCCCCCCC		38.0354558025
372PhosphorylationSRPARGLYSRSGSLS
CCCCCCCCCCCCCCC		12.5929514104
375PhosphorylationARGLYSRSGSLSGRS
CCCCCCCCCCCCCCH		27.1330635358
377PhosphorylationGLYSRSGSLSGRSSL
CCCCCCCCCCCCHHH		22.1727149854
379PhosphorylationYSRSGSLSGRSSLRG
CCCCCCCCCCHHHCC		33.5827600695
382PhosphorylationSGSLSGRSSLRGEAE
CCCCCCCHHHCCCCC		36.9328833060
383PhosphorylationGSLSGRSSLRGEAEN
CCCCCCHHHCCCCCC		22.2628833060
392PhosphorylationRGEAENATEVSTVLK
CCCCCCCCEEEEEEE		48.8028833060
451AcetylationLCALKFLKLEDFLDN
CCHHEEECHHHHHCC		53.62-
498PhosphorylationQRQKKIFSKQQGKAF
HHHHHHCHHHHHHHH		32.7825266776
528PhosphorylationLLRRLIPSAVATGTF
HHHHHCCCHHHCCCC		28.5125619855
532PhosphorylationLIPSAVATGTFSPNA
HCCCHHHCCCCCCCC		30.1025619855
534PhosphorylationPSAVATGTFSPNASP
CCHHHCCCCCCCCCC		19.3125619855
536PhosphorylationAVATGTFSPNASPGA
HHHCCCCCCCCCCCC		19.6526824392
540PhosphorylationGTFSPNASPGAEIRH
CCCCCCCCCCCEEEE		30.4326824392
562PhosphorylationKLNLGADSDSSSQKS
EECCCCCCCCCCCCC		38.5725338131
565PhosphorylationLGADSDSSSQKSPPG
CCCCCCCCCCCCCCC		41.6025338131
569PhosphorylationSDSSSQKSPPGLPST
CCCCCCCCCCCCCCC		28.7926643407
575PhosphorylationKSPPGLPSTSCSLSS
CCCCCCCCCCCCCCC		37.6926643407
576PhosphorylationSPPGLPSTSCSLSSP
CCCCCCCCCCCCCCC		31.6426643407
577PhosphorylationPPGLPSTSCSLSSPT
CCCCCCCCCCCCCCC		13.1726643407
579PhosphorylationGLPSTSCSLSSPTHE
CCCCCCCCCCCCCCC		30.9326643407
581PhosphorylationPSTSCSLSSPTHEST
CCCCCCCCCCCCCCC		20.2726643407
582PhosphorylationSTSCSLSSPTHESTT
CCCCCCCCCCCCCCC		38.8326643407
584PhosphorylationSCSLSSPTHESTTSP
CCCCCCCCCCCCCCC		39.9826643407
587PhosphorylationLSSPTHESTTSPELP
CCCCCCCCCCCCCCC		29.4026643407
588PhosphorylationSSPTHESTTSPELPS
CCCCCCCCCCCCCCC		28.4526643407
589PhosphorylationSPTHESTTSPELPSE
CCCCCCCCCCCCCCC		52.1126643407
590PhosphorylationPTHESTTSPELPSET
CCCCCCCCCCCCCCC		19.2326643407
595PhosphorylationTTSPELPSETQETPG
CCCCCCCCCCCCCCC		66.9422942356
597PhosphorylationSPELPSETQETPGPG
CCCCCCCCCCCCCCC		35.7222942356
607PhosphorylationTPGPGLCSPLRKSPL
CCCCCCCCCCCCCCC		31.8225266776
612PhosphorylationLCSPLRKSPLTLEDF
CCCCCCCCCCCHHHH		20.7827180971
615PhosphorylationPLRKSPLTLEDFKFL
CCCCCCCCHHHHHHH		31.3329472430
772PhosphorylationLCKEGMGYGDRTSTF
CCCCCCCCCCCCCCC		13.6322322096
776PhosphorylationGMGYGDRTSTFCGTP
CCCCCCCCCCCCCCC		36.5422322096
777PhosphorylationMGYGDRTSTFCGTPE
CCCCCCCCCCCCCCH		22.0022322096
778PhosphorylationGYGDRTSTFCGTPEF
CCCCCCCCCCCCCHH		23.4922322096
782PhosphorylationRTSTFCGTPEFLAPE
CCCCCCCCCHHHCCH		22.3322322096
792PhosphorylationFLAPEVLTDTSYTRA
HHCCHHHCCCCCHHH		42.2723984901
794PhosphorylationAPEVLTDTSYTRAVD
CCHHHCCCCCHHHHH		20.5623984901
838PhosphorylationIVNDEVRYPRFLSAE
HHCCCCCCCCCCCHH		12.1622871156
903PhosphorylationVPTLSGRTDVSNFDE
CCCCCCCCCCCCCCH		44.2525619855
906PhosphorylationLSGRTDVSNFDEEFT
CCCCCCCCCCCHHHC		34.2925777480
913PhosphorylationSNFDEEFTGEAPTLS
CCCCHHHCCCCCCCC		37.0725619855
918PhosphorylationEFTGEAPTLSPPRDA
HHCCCCCCCCCCCCC		47.0924925903
920PhosphorylationTGEAPTLSPPRDARP
CCCCCCCCCCCCCCC		35.0224925903
929PhosphorylationPRDARPLTAAEQAAF
CCCCCCCCHHHHHHH		26.8926160508
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
778TPhosphorylationKinasePDPK1Q9Z2A0
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKN1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PKN1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PKN1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PKN1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory